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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Dynamics and orientation of N~+(CD_3)_3~- bromoacetylcholine bound to its binding site on the nicotinic acetylcholine receptor
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Dynamics and orientation of N~+(CD_3)_3~- bromoacetylcholine bound to its binding site on the nicotinic acetylcholine receptor

机译：N〜+（CD_3）_3〜-溴乙酰胆碱与其烟碱乙酰胆碱受体结合位点结合的动力学和方向

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摘要

Dynamic and structural information has been obtained for an analogue of acetylcholine while bound to the agonist binding site on the nicotinic acetylcholine receptor (nAcChoR), using wide-line deuterium solid-state NMR. Analysis of the deuterium lineshape obtained at various temperatures from unoriented nAcChoR mem- branes labeled with deuterated bromoacetylcholine (BAC) showed that the quaternary ammonium group of the ligand is well con- strained within the agonist binding site when compared with the dynamics observed in the crystalline solids. This motional restric- tion would suggest that a high degree of complementarity exists between the quaternary ammonium group of the ligand and the protein within the agonist binding site. nAcChoR membranes were uniaxially oriented by isopotential centrifugation as determined by phosphorous NMR of the membrane phospholipids. Analysis of the deuterium NMR lineshape of these oriented membranes enriched with the nAcChoR labeled with N~+(CD_3)_3-BAC has enabled us to determine that the angle formed between the quaternary ammo- nium group of the BAC and the membrane normal is 42" in the desensitized form of the receptor. This measurement allows us to orient in part the bound ligand within the proposed receptor binding site.
机译：使用宽线氘核固态NMR，已获得与乙酰胆碱类似物结合到烟碱乙酰胆碱受体（nAcChoR）上激动剂结合位点的动力学和结构信息。对氘化溴乙酰胆碱（BAC）标记的未取向nAcChoR膜在不同温度下获得的氘线形的分析表明，与晶体中观察到的动力学相比，配体的季铵基团被很好地限制在激动剂结合位点内。固体。这种运动限制表明，配体的季铵基团与激动剂结合位点内的蛋白质之间存在高度的互补性。通过等电位离心将nAcChoR膜单轴定向，这是通过膜磷脂的磷NMR测定的。分析这些富含NAc +（CD_3）_3-BAC的nAcChoR的取向膜的氘核NMR线形，使我们能够确定BAC的季铵基团与膜法线之间形成的夹角为42该测量使我们能够使所提议的受体结合位点内的结合配体部分定向。

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